CPLM-002774

Genbank Nucleotide ID

Phosphoglycerate kinase 1

Protein Synonyms/Alias

Mus musculus (Mouse)

Position	Peptide	Type	References
6	**MSLSNKLTLDKLD	acetylation	[1, 2]
6	**MSLSNKLTLDKLD	succinylation	[2]
6	**MSLSNKLTLDKLD	ubiquitination	[3]
11	SNKLTLDKLDVKGKR	acetylation	[1, 2, 4, 5]
11	SNKLTLDKLDVKGKR	succinylation	[2]
11	SNKLTLDKLDVKGKR	ubiquitination	[3]
15	TLDKLDVKGKRVVMR	ubiquitination	[3]
30	VDFNVPMKNNQITNN	ubiquitination	[3]
41	ITNNQRIKAAVPSIK	acetylation	[1]
48	KAAVPSIKFCLDNGA	acetylation	[1, 2, 6]
48	KAAVPSIKFCLDNGA	succinylation	[2]
48	KAAVPSIKFCLDNGA	ubiquitination	[3]
75	DGVPMPDKYSLEPVA	acetylation	[1, 2, 5, 7]
75	DGVPMPDKYSLEPVA	ubiquitination	[3]
86	EPVAAELKSLLGKDV	acetylation	[1]
86	EPVAAELKSLLGKDV	ubiquitination	[3]
91	ELKSLLGKDVLFLKD	acetylation	[1, 2, 4, 5, 8]
91	ELKSLLGKDVLFLKD	succinylation	[2]
91	ELKSLLGKDVLFLKD	ubiquitination	[3]
131	FHVEEEGKGKDASGN	acetylation	[4, 8]
141	DASGNKVKAEPAKID	acetylation	[4, 6]
141	DASGNKVKAEPAKID	ubiquitination	[3]
146	KVKAEPAKIDAFRAS	acetylation	[4]
146	KVKAEPAKIDAFRAS	ubiquitination	[3]
156	AFRASLSKLGDVYVN	ubiquitination	[3]
184	VGVNLPQKAGGFLMK	ubiquitination	[3]
191	KAGGFLMKKELNYFA	acetylation	[2]
191	KAGGFLMKKELNYFA	succinylation	[2]
192	AGGFLMKKELNYFAK	acetylation	[2]
192	AGGFLMKKELNYFAK	succinylation	[2]
192	AGGFLMKKELNYFAK	ubiquitination	[3]
216	LAILGGAKVADKIQL	acetylation	[5]
216	LAILGGAKVADKIQL	ubiquitination	[3]
220	GGAKVADKIQLINNM	acetylation	[1, 5]
220	GGAKVADKIQLINNM	ubiquitination	[3]
264	LYDEEGAKIVKDLMS	acetylation	[5]
264	LYDEEGAKIVKDLMS	ubiquitination	[3]
267	EEGAKIVKDLMSKAE	ubiquitination	[3]
272	IVKDLMSKAEKNGVK	acetylation	[1]
272	IVKDLMSKAEKNGVK	ubiquitination	[3]
279	KAEKNGVKITLPVDF	ubiquitination	[3]
291	VDFVTADKFDENAKT	acetylation	[1, 2, 5, 8]
291	VDFVTADKFDENAKT	ubiquitination	[3]
323	CGTESSKKYAEAVGR	acetylation	[1, 2, 8]
323	CGTESSKKYAEAVGR	ubiquitination	[3]
353	EAFARGTKSLMDEVV	acetylation	[2, 5]
353	EAFARGTKSLMDEVV	ubiquitination	[3]
361	SLMDEVVKATSRGCI	acetylation	[1, 2, 5, 8]
361	SLMDEVVKATSRGCI	succinylation	[2]
361	SLMDEVVKATSRGCI	ubiquitination	[3]
388	AKWNTEDKVSHVSTG	acetylation	[2, 5]
388	AKWNTEDKVSHVSTG	ubiquitination	[3]

[1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[7] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
[8] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]

Functional Description

NP_BIND 373 376 ATP (By similarity).
REGION 24 26 Substrate binding (By similarity).
REGION 63 66 Substrate binding (By similarity).
BINDING 39 39 Substrate (By similarity).
BINDING 123 123 Substrate (By similarity).
BINDING 171 171 Substrate (By similarity).
BINDING 220 220 ATP (By similarity).
BINDING 313 313 ATP; via carbonyl oxygen (By similarity).
BINDING 344 344 ATP (By similarity).
MOD_RES 2 2 N-acetylserine (By similarity).
MOD_RES 11 11 N6-acetyllysine (By similarity).
MOD_RES 48 48 N6-acetyllysine (By similarity).
MOD_RES 75 75 N6-acetyllysine (By similarity).
MOD_RES 76 76 Phosphotyrosine.
MOD_RES 86 86 N6-acetyllysine (By similarity).
MOD_RES 97 97 N6-acetyllysine (By similarity).
MOD_RES 131 131 N6-acetyllysine; alternate (By
MOD_RES 131 131 N6-malonyllysine; alternate (By
MOD_RES 146 146 N6-acetyllysine (By similarity).
MOD_RES 196 196 Phosphotyrosine.
MOD_RES 199 199 N6-acetyllysine (By similarity).
MOD_RES 203 203 Phosphoserine.
MOD_RES 267 267 N6-acetyllysine (By similarity).
MOD_RES 291 291 N6-acetyllysine (By similarity).
MOD_RES 390 390 Phosphoserine.

Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; ISS:UniProtKB.
GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway.

IPR001576; Phosphoglycerate_kinase.
IPR015901; Phosphoglycerate_kinase_C.
IPR015911; Phosphoglycerate_kinase_CS.
IPR015824; Phosphoglycerate_kinase_N.

PS00111; PGLYCERATE_KINASE

PR00477; PHGLYCKINASE.